Analytical Data
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Gene name
tdh1
- Application
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Alternative Names
(Kanagawa phenomenon-associated hemolysin)
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Species
Vibrio parahaemolyticus serotype O3:K6
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P19249
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Expression Region
25-189aa
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Molecular Weight
26.0 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
TDH1, or Tridactylus dorsalis histone 1, is an intriguing recombinant protein that has garnered attention in the field of molecular biology and biotechnology. This protein is derived from the trilobite crustacean known for its unique evolutionary adaptations, providing insights into historical genetic mechanisms. Research into TDH1 focuses on its structure, function, and potential applications, particularly in understanding the role of histones in gene regulation and chromatin architecture. Histone proteins are crucial for DNA packaging in cells, and the study of TDH1 offers a novel perspective on how ancient proteins can contribute to contemporary biological processes. Furthermore, the ability to produce TDH1 as a recombinant protein allows for detailed analysis of its biochemical properties and interactions within cellular systems, which may lead to innovative biotechnological applications. These may include therapeutic uses, where TDH1's unique features can be harnessed for drug delivery systems or as part of gene expression regulation tools. Overall, the investigation of TDH1 as a recombinant protein holds promise for advancing our understanding of both evolutionary biology and practical applications in genetic engineering and biotechnology.
